Backbone assignment of the UHM domain of Puf60 free and bound to five ligands

Lorenzo Corsini; Michael Sattler

doi:10.1007/s12104-008-9123-7

Backbone assignment of the UHM domain of Puf60 free and bound to five ligands

Lorenzo Corsini
, Michael Sattler

Lehrstuhl für Biomolekulare NMR-Spektroskopie

Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

4 Zitate (Scopus)

Abstract

U2AF homology motifs (UHM) are protein domains that bind peptidic UHM ligand motifs (ULM) and thus form an intricate network of interactions involved in splicing regulation. Here, we report the backbone assignment of the UHM domain of the splicing factor Puf60 as well as ¹H, ¹⁵N chemical shifts upon binding of the ULM peptides U2AF ⁶⁵ (85-112), SF1 (1-25), SF3b155 (194-229), SF3b155 (317-357), and Prp16 (201-238).

Originalsprache	Englisch
Seiten (von - bis)	211-214
Seitenumfang	4
Fachzeitschrift	Biomolecular NMR Assignments
Jahrgang	2
Ausgabenummer	2
DOIs	https://doi.org/10.1007/s12104-008-9123-7
Publikationsstatus	Veröffentlicht - Dez. 2008

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title = "Backbone assignment of the UHM domain of Puf60 free and bound to five ligands",

abstract = "U2AF homology motifs (UHM) are protein domains that bind peptidic UHM ligand motifs (ULM) and thus form an intricate network of interactions involved in splicing regulation. Here, we report the backbone assignment of the UHM domain of the splicing factor Puf60 as well as 1H, 15N chemical shifts upon binding of the ULM peptides U2AF 65 (85-112), SF1 (1-25), SF3b155 (194-229), SF3b155 (317-357), and Prp16 (201-238).",

keywords = "Alternative splicing, Chemical shift perturbation, FBP interacting repressor, Splicing, UHM, ULM",

author = "Lorenzo Corsini and Michael Sattler",

note = "Funding Information: Acknowledgments This work was supported by the Deutsche Forschungsgemeinschaft (Sa 823/5) and EC (3D Repertoire, LSHG-CT–2005–512028).",

year = "2008",

month = dec,

doi = "10.1007/s12104-008-9123-7",

language = "English",

volume = "2",

pages = "211--214",

journal = "Biomolecular NMR Assignments",

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T1 - Backbone assignment of the UHM domain of Puf60 free and bound to five ligands

AU - Corsini, Lorenzo

AU - Sattler, Michael

N1 - Funding Information: Acknowledgments This work was supported by the Deutsche Forschungsgemeinschaft (Sa 823/5) and EC (3D Repertoire, LSHG-CT–2005–512028).

PY - 2008/12

Y1 - 2008/12

N2 - U2AF homology motifs (UHM) are protein domains that bind peptidic UHM ligand motifs (ULM) and thus form an intricate network of interactions involved in splicing regulation. Here, we report the backbone assignment of the UHM domain of the splicing factor Puf60 as well as 1H, 15N chemical shifts upon binding of the ULM peptides U2AF 65 (85-112), SF1 (1-25), SF3b155 (194-229), SF3b155 (317-357), and Prp16 (201-238).

AB - U2AF homology motifs (UHM) are protein domains that bind peptidic UHM ligand motifs (ULM) and thus form an intricate network of interactions involved in splicing regulation. Here, we report the backbone assignment of the UHM domain of the splicing factor Puf60 as well as 1H, 15N chemical shifts upon binding of the ULM peptides U2AF 65 (85-112), SF1 (1-25), SF3b155 (194-229), SF3b155 (317-357), and Prp16 (201-238).

KW - Alternative splicing

KW - Chemical shift perturbation

KW - FBP interacting repressor

KW - Splicing

KW - UHM

KW - ULM

UR - https://www.scopus.com/pages/publications/68849100480

U2 - 10.1007/s12104-008-9123-7

DO - 10.1007/s12104-008-9123-7

M3 - Article

C2 - 19636907

AN - SCOPUS:68849100480

SN - 1874-2718

VL - 2

SP - 211

EP - 214

JO - Biomolecular NMR Assignments

JF - Biomolecular NMR Assignments

IS - 2

ER -

Backbone assignment of the UHM domain of Puf60 free and bound to five ligands

Abstract

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